Article (Scientific journals)
Crystallographic mapping of β-lactams bound to a D-alanyl-D-alanine peptidase target enzyme
Kelly, Judith A.; Knox, James R.; Zhao, Haiching C. et al.
1989In Journal of Molecular Biology, 209 (2), p. 281-295
Peer Reviewed verified by ORBi
 

Files


Full Text
GHUYSEN_1989_1347.pdf
Publisher postprint (936.12 kB)
Download

All documents in ORBi are protected by a user license.

Send to



Details



Keywords :
Lactam; Bacteria; Actinomycetes; Actinomycetales; Streptomycetaceae; Enzyme; Antibiotic; Streptomyces; Cell wall; Computer aided analysis; Electron density map; X ray diffraction; Crystallography; Conserved sequence; Active site; Hydrogen bond; Cephalosporin derivatives; Penicillin derivatives; Inhibitor enzyme complex; Substrate enzyme complex; Peptidase; Molecular interaction; Lactame; Bactérie; D-Dpeptidase; Antibiotique; Paroi cellulaire; Analyse assistée; Diagramme densité électronique; Diffraction RX; Cristallographie; Séquence conservée; Site actif; Liaison hydrogène; Céphalosporine dérivé; Pénicilline dérivé; Complexe enzyme inhibiteur; Complexe enzyme substrat; Interaction moléculaire
Abstract :
[en] X-ray crystallography has been used to examine the binding of three members of the beta-lactam family of antibiotics to the D-alanyl-D-alanine peptidase from Streptomyces R61, a target of penicillins. Cephalosporin C, the monobactam analog of penicillin G and (2,3)-alpha-methylene benzylpenicillin have been mapped at 2.3 A resolution in the form of acyl-enzyme complexes bound to serine 62. On the basis of the positions of these inhibitors, the binding of a tripeptide substrate for the enzyme, L-lysyl-D-alanyl-D-alanine, has been modeled in the active site. The binding of both inhibitors and substrate is facilitated by hydrogen-bonding interactions with a conserved beta-strand (297-303), which is antiparallel to the beta-lactam's acylamide linkage or the substrate's peptide bond. The active site is similar to that in beta-lactamases.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Kelly, Judith A.;  University of Connecticut - UCONN > Institute of Material Science > Department of Molecular And Cell Biology
Knox, James R.;  University of Connecticut - UCONN > Institute of Material Science > Department of Molecular And Cell Biology
Zhao, Haiching C.;  University of Connecticut - UCONN > Institute of Material Science > Department of Molecular And Cell Biology
Frère, Jean-Marie ;  Université de Liège - ULiège
Ghuysen, Jean-Marie ;  Université de Liège - ULiège > Institut de Chimie > Service de Microbiologie
Language :
English
Title :
Crystallographic mapping of β-lactams bound to a D-alanyl-D-alanine peptidase target enzyme
Publication date :
1989
Journal title :
Journal of Molecular Biology
ISSN :
0022-2836
eISSN :
1089-8638
Publisher :
Academic Press, London, United Kingdom
Volume :
209
Issue :
2
Pages :
281-295
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 25 May 2011

Statistics


Number of views
105 (0 by ULiège)
Number of downloads
377 (1 by ULiège)

Scopus citations®
 
87
Scopus citations®
without self-citations
56
OpenCitations
 
82

Bibliography


Similar publications



Contact ORBi